Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 고성호 | - |
dc.date.accessioned | 2019-12-03T05:12:35Z | - |
dc.date.available | 2019-12-03T05:12:35Z | - |
dc.date.issued | 2017-12 | - |
dc.identifier.citation | Dementia and Neurocognitive Disorders(대한치매학회지), v. 16, no. 4, page. 121-127 | en_US |
dc.identifier.issn | 1738-1495 | - |
dc.identifier.issn | 2384-0757 | - |
dc.identifier.uri | https://dnd.or.kr/DOIx.php?id=10.12779/dnd.2017.16.4.121 | - |
dc.identifier.uri | https://repository.hanyang.ac.kr/handle/20.500.11754/116821 | - |
dc.description.abstract | Background and Purpose Amyloid beta (Aβ) is the main component of amyloid plaques, which are deposited in the brains of patients with Alzheimer’s disease (AD). Biochemical and animal studies support the central role of Aβ in AD pathogenesis. Despite several investigations focused on the pathogenic mechanisms of Aβ, it is still unclear how Aβ accumulates in the central nervous system and subsequently initiates the disease at the cellular level. In this study, we investigated the pathogenic mechanisms of Aβ using proteomics and antibody microarrays. Methods To evaluate the effect of Aβ on neural stem cells (NSCs), we treated primary cultured cortical NSCs with several doses of Aβ for 48 h. A 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazolium bromide assay, trypan blue staining, and bromodeoxyuridine cell proliferation assay were performed. We detected several intracellular proteins that may be associated with Aβ by proteomics and Western blotting analysis. Results Various viability tests showed that Aβ decreased NSCs viability and cell proliferation in a concentration-dependent manner. Aβ treatment significantly decreased lactate dehydrogenase B, high-mobility group box 1, aldolase C, Ezrin, and survival signals including phosphorylated phosphoinositide 3-kinase, Akt, and glycogen synthase kinase-3β. Conclusions These results suggest that several factors determined by proteomics and Western blot hold the clue to Aβ pathogenesis. Further studies are required to investigate the role of these factors. | en_US |
dc.description.sponsorship | This work was supported by the Basic Science Research Program of theNational Research Foundation of Korea funded by the Ministry of Science,ICT and Future Planning (2015R1A2A2A04004865), the Korea HealthTechnology R&D Project through the Korea Health Industry Development Institute (KHIDI), the Ministry of Health & Welfare, Republic of Korea (grant number: HI17C2160), the Korea Drug Development Fund(KDDF) funded by the Ministry of Science and ICT, Ministry of Trade, Industry & Energy, and Ministry of Health & Welfare (KDDF-201609-02, Republic of Korea), and by the Medical Research Center (2017R1A5A2015395). | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | 대한치매학회 | en_US |
dc.subject | amyloid beta | en_US |
dc.subject | neural stem cells | en_US |
dc.subject | proteomics | en_US |
dc.title | Neural Stem Cell Death Mechanisms Induced by Amyloid Beta | en_US |
dc.type | Article | en_US |
dc.relation.no | 4 | - |
dc.relation.volume | 16 | - |
dc.identifier.doi | 10.12779/dnd.2017.16.4.121 | - |
dc.relation.page | 121-127 | - |
dc.relation.journal | Dementia and Neurocognitive Disorders(대한치매학회지) | - |
dc.contributor.googleauthor | Lee, Jongmin | - |
dc.contributor.googleauthor | Park, Hyun-Hee | - |
dc.contributor.googleauthor | Koh, Seong-Ho | - |
dc.contributor.googleauthor | Choi, Hojin | - |
dc.relation.code | 2017019278 | - |
dc.sector.campus | S | - |
dc.sector.daehak | COLLEGE OF MEDICINE[S] | - |
dc.sector.department | DEPARTMENT OF MEDICINE | - |
dc.identifier.pid | ksh213 | - |
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